ArticleJournal of virology2013
A mutant influenza virus that uses an N1 neuraminidase as the receptor-binding protein.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 98 citations in OpenAlex.
- Defining the molecular interaction between influenza hemagglutinin and MHC-II.bioRxiv : the preprint server for biology · 2026Article
- Cross-reactive human antibody responses to H5N1 influenza virus neuraminidase are shaped by immune history.Nature communications · 2026Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza haemagglutinin.Nature ecology & evolution · 2026Article
- A protective and heterosubtypic antibody lineage targeting the influenza A virus neuraminidase active site.The Journal of clinical investigation · 2025Article
- Pleiotropic mutational effects on function and stability constrain the antigenic evolution of influenza hemagglutinin.bioRxiv : the preprint server for biology · 2025Article
- RSV F evolution escapes some monoclonal antibodies but does not strongly erode neutralization by human polyclonal sera.Journal of virology · 2025Article
- Avian Influenza Virus: Comparative Evolution as the Key for Predicting Host Tropism Expansion.Pathogens (Basel, Switzerland) · 2025Article
- RSV F evolution escapes some monoclonal antibodies but does not strongly erode neutralization by human polyclonal sera.bioRxiv : the preprint server for biology · 2025Article
- Deep mutational scanning of H5 hemagglutinin to inform influenza virus surveillance.PLoS biology · 2024Article
- High-throughput sequencing-based neutralization assay reveals how repeated vaccinations impact titers to recent human H1N1 influenza strains.Journal of virology · 2024Article
- Age-dependent heterogeneity in the antigenic effects of mutations to influenza hemagglutinin.Cell host & microbe · 2024Article
- Exploring Potential Intermediates in the Cross-Species Transmission of Influenza A Virus to Humans.Viruses · 2024Review
- High-throughput sequencing-based neutralization assay reveals how repeated vaccinations impact titers to recent human H1N1 influenza strains.bioRxiv : the preprint server for biology · 2024Article
- Age-dependent heterogeneity in the antigenic effects of mutations to influenza hemagglutinin.bioRxiv : the preprint server for biology · 2023Article
- Receptor Binding Properties of Neuraminidase for influenza A virus: An Overview of Recent Research Advances.Virulence · 2023Review
- An atlas of continuous adaptive evolution in endemic human viruses.Cell host & microbe · 2023Article
- New insights into the neuraminidase-mediated hemagglutination activity of influenza A(H3N2) viruses.Antiviral research · 2023Article
- Avian Influenza Virus Tropism in Humans.Viruses · 2023Review
- Phenotypic effects of mutations observed in the neuraminidase of human origin H5N1 influenza A viruses.PLoS pathogens · 2023Article
- Quantitative structural analysis of influenza virus by cryo-electron tomography and convolutional neural networks.Structure (London, England : 1993) · 2022Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
In the vast majority of influenza A viruses characterized to date, hemagglutinin (HA) is the receptor-binding and fusion protein, whereas neuraminidase (NA) is a receptor-cleaving protein that facilitates viral release but is expendable for entry. However, the NAs of some recent human H3N2 isolates have acquired receptor-binding activity via the mutation D151G, although these isolates also appear to retain the ability to bind receptors via HA. We report here the laboratory generation of a mutation (G147R) that enables an N1 NA to completely co-opt the receptor-binding function normally performed by HA. Viruses with this mutant NA grow to high titers even in the presence of extensive mutations to conserved residues in HA's receptor-binding pocket. When the receptor-binding NA is paired with this binding-deficient HA, viral infectivity and red blood cell agglutination are blocked by NA inhibitors. Furthermore, virus-like particles expressing only the receptor-binding NA agglutinate red blood cells in an NA-dependent manner. Although the G147R NA receptor-binding mutant virus that we characterize is a laboratory creation, this same mutation is found in several natural clusters of H1N1 and H5N1 viruses. Our results demonstrate that, at least in tissue culture, influenza virus receptor-binding activity can be entirely shifted from HA to NA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.